ArticleActa crystallographica. Section F, Structural biology communications2014
Expression, purification, crystallization and preliminary crystallographic study of the cytoplasmic domain of the mitochondrial dynamics protein MiD51.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 1 citations in OpenAlex.
- MiD49 and MiD51: New mediators of mitochondrial fission and novel targets for cardioprotection.Conditioning medicine · 2018Article
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2 authors at 2 institutions in 1 country.
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Abstract
Mitochondria play central roles in many cellular and physiological processes. They are highly dynamic organelles and continually undergo fusion and fission. Mitochondrial dynamics protein 51 kDa (MiD51), an integral mitochondrial outer membrane protein, recruits dynamin-related protein 1 (Drp1; a mitochondrial fission protein) to mitochondria and facilitates Drp1-directed mitochondrial fission. In this study, the cytoplasmic domain of MiD51 was overexpressed in Escherichia coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 3.1 Å and the crystal belonged to space group P41212, with unit-cell parameters a = b = 90.1, c = 124.7 Å, α = β = γ = 90°. The asymmetric unit had the highest probability of containing one molecule, with a Matthews coefficient of 3.32 Å(3) Da(-1) and a solvent content of 63.0%.
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